| pubmed-article:3057494 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3057494 | lifeskim:mentions | umls-concept:C1706586 | lld:lifeskim |
| pubmed-article:3057494 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:3057494 | lifeskim:mentions | umls-concept:C0010834 | lld:lifeskim |
| pubmed-article:3057494 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:3057494 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:3057494 | lifeskim:mentions | umls-concept:C0029005 | lld:lifeskim |
| pubmed-article:3057494 | lifeskim:mentions | umls-concept:C0442805 | lld:lifeskim |
| pubmed-article:3057494 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
| pubmed-article:3057494 | lifeskim:mentions | umls-concept:C0812215 | lld:lifeskim |
| pubmed-article:3057494 | lifeskim:mentions | umls-concept:C0018284 | lld:lifeskim |
| pubmed-article:3057494 | lifeskim:mentions | umls-concept:C2746015 | lld:lifeskim |
| pubmed-article:3057494 | lifeskim:mentions | umls-concept:C1150527 | lld:lifeskim |
| pubmed-article:3057494 | pubmed:issue | 23 | lld:pubmed |
| pubmed-article:3057494 | pubmed:dateCreated | 1988-12-30 | lld:pubmed |
| pubmed-article:3057494 | pubmed:abstractText | We have examined the phosphorylation and the serine/threonine-specific kinase activity of the protooncogene product Raf-1 (formerly c-raf) in response to oncogenic transformation or growth-factor treatment of mouse 3T3 cells. Expression of the membrane-bound oncogene products encoded by v-fms, v-src, v-sis, polyoma virus middle-sized tumor antigen, and Ha-ras increased the apparent molecular weight and phosphorylation of the Raf-1 protein, while expression of the nuclear oncogene and protooncogene products encoded by v-fos and c-myc did not. Changes in electrophoretic mobility and phosphorylation occurred rapidly in response to treatment of cells with platelet-derived growth factor, acidic fibroblast growth factor, epidermal growth factor, and the protein kinase C activator phorbol 12-myristate 13-acetate, but not insulin. The phosphorylation of the Raf-1 protein occurred primarily on serine and threonine residues. However, a subpopulation of Raf-1 molecules was phosphorylated on tyrosine residues in cells transformed by v-src or stimulated with platelet-derived growth factor. Transformation by v-src, or treatment with platelet-derived growth factor or phorbol 12-myristate 13-acetate, activated the Raf-1-associated serine/kinase activity as measured in immune-complex kinase assays. These findings suggest that proliferative signals generated at the membrane result in the phosphorylation of the Raf-1 protein and the activation of its serine/threonine kinase activity. Raf-1 activation may thus serve to transduce signals from the membrane to the cytoplasm and perhaps on to the nucleus. | lld:pubmed |
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| pubmed-article:3057494 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:3057494 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3057494 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3057494 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:3057494 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:3057494 | pubmed:author | pubmed-author:RobertsT MTM | lld:pubmed |
| pubmed-article:3057494 | pubmed:author | pubmed-author:RappUU | lld:pubmed |
| pubmed-article:3057494 | pubmed:author | pubmed-author:KaplanD RDR | lld:pubmed |
| pubmed-article:3057494 | pubmed:author | pubmed-author:MorrisonD KDK | lld:pubmed |
| pubmed-article:3057494 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3057494 | pubmed:volume | 85 | lld:pubmed |
| pubmed-article:3057494 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3057494 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3057494 | pubmed:pagination | 8855-9 | lld:pubmed |
| pubmed-article:3057494 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:3057494 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3057494 | pubmed:articleTitle | Signal transduction from membrane to cytoplasm: growth factors and membrane-bound oncogene products increase Raf-1 phosphorylation and associated protein kinase activity. | lld:pubmed |
| pubmed-article:3057494 | pubmed:affiliation | Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115. | lld:pubmed |
| pubmed-article:3057494 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3057494 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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